desmin

When the gene for desmin is knocked out it is no longer able to function properly.

The presence of desmin and myogenin can be detected using immunohistochemistry.

Finally, desmin may be important in mitochondria function.

Desmin is also important in muscle cell architecture and structure since it connects many components of the cytoplasm.

They are both vimentin and desmin positive.

More research needs to be done on desmin's expression and interactions in the muscle cell in order to determine its exact function.

Desmin is an intermediate filament protein, which is linked to the desmosomes.

Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms.

They typically stain with CD34 and desmin.

Later, a yeast two-hybrid method was used to demonstrate that syncoilin is a binding partner of desmin.

Electron microscopic analysis shows that desmuslin colocalizes with desmin, another muscle IF protein.

The function of desmin has been deduced through studies in knockout mice, but the underlying mechanism of its action is not known.

Subtype B accounts for the rest of the pericytes and has desmin and alpha smooth muscles.

When desmin is not functioning properly there is improper mitochondrial distribution, number, morphology and function.

Desmin is a protein that in humans is encoded by the DES gene.

Activated satellite cells also begin expressing muscle-specific filament proteins such as desmin as they differentiate.

Recently it could be shown, that mutations in the desmin gene could cause ARVC.

Desmin is a type III intermediate filament found near the Z line in sarcomeres.

They were also negative for neuroectodermal, epithelial, and muscle cell markers including nestin, pancytokeratin, and desmin (data not shown).

Mutations of several other Z-disk related proteins, such as desmin, alfa-B-crystallin and myotilin can cause disorders similar to zaspopathy.

Desmin is one of the earliest protein markers for muscle tissue in embryogenesis as it is detected in the somites.

Rhabdomyoblasts and poorly differentiated small cells display positivity for desmin and myosin while neural areas are variably sensitive to S-100.

Through its connection to the sarcomere Desmin connects the contractile apparatus to the cell nucleus, mitochondria, and post-synaptic areas of motor endplates.

It is closely related to its non-epithelial family members, vimentin, desmin, and peripherin, which are all involved in the structure and function of the cell's cytoskeleton.

Since desmin is expressed at a low level during differentiation another protein may be able to compensate for desmin's function early in development but not later on.